About: Molecular studies of the asymmetric pore structure of the human cardiac voltage- dependent Ca2+ channel. Conserved residue, Glu-1086, regulates proton-dependent ion permeation

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About: Molecular studies of the asymmetric pore structure of the human cardiac voltage- dependent Ca2+ channel. Conserved residue, Glu-1086, regulates proton-dependent ion permeation Goto Sponge NotDistinct Permalink

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scientific article published on 01 September 1996

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована у вересні 1996 (uk) im September 1996 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en setiembre de 1996 (ast) scientific article published on 01 September 1996 (en)
publication date	wds:Q71514572-AF9A350A-49E3-4AF2-9CC3-789DA93F2C37
publication date	1996-09-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q71514572-09E86E18-6AC6-42A2-8AB2-1AF400DC4DA5
language of work or name	English
cites work	wds:Q71514572-1986747A-1F94-4CF9-8068-EB1048ED1984 wds:Q71514572-1CE4F491-96F2-408F-B3F8-B0E52A53A941 wds:Q71514572-2A0FAEC9-ACE9-41D3-9E14-23EF8E57E011 wds:Q71514572-3E439B14-9F30-4F72-B9D2-889437874624 wds:Q71514572-48A581A8-CB29-440F-A5CA-E0C638A27D7B wds:Q71514572-584D937D-9C05-4E2E-BE39-8E68993DFE8B wds:Q71514572-5FD3B12C-F258-4A1D-AF08-62380E7A5E6C wds:Q71514572-7B32EB52-50E6-4BC2-BF63-66AA2BFEFC8A wds:Q71514572-85664485-A101-40AD-8FFF-71E3823C6A65 wds:Q71514572-9414F20D-5355-4550-B43E-9BB77DB140EF wds:Q71514572-9659E4FE-E9FB-41E0-8160-558A8B9B9725 wds:Q71514572-96F7A55E-0A55-49C8-BC5C-5F701F68D574 wds:Q71514572-9A020C58-B934-4FBD-97C4-935C920FB270 wds:Q71514572-C88876AE-94CB-4BC7-8870-A6731DC20C0D wds:Q71514572-CA20659B-25D8-485E-B23A-897FBB9D9DF7 wds:Q71514572-DAF43601-4D9D-46F7-A282-C1BBE2D44B3A wds:Q71514572-DCE5263D-6E2A-457D-93B4-CC291B24DF9A wds:Q71514572-F3788BE9-C778-4A1E-B04B-799D780D79DD wds:Q71514572-FBC9C57B-EDB2-4AB8-81E7-2BE9320DD2FC
cites work	Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches Cloning, chromosomal localization, and functional expression of the alpha 1 subunit of the L-type voltage-dependent calcium channel from normal human heart Molecular determinants of Ca2+ selectivity and ion permeation in L-type Ca2+ channels Involvement of the carboxyl-terminal region of the alpha 1 subunit in voltage-dependent inactivation of cardiac calcium channels Ca2+ channel selectivity at a single locus for high-affinity Ca2+ interactions Sequence and expression of mRNAs encoding the alpha 1 and alpha 2 subunits of a DHP-sensitive calcium channel Electrostatic effects in proteins Calcium binding in the pore of L-type calcium channels modulates high affinity dihydropyridine binding Interactions of protons with single open L-type calcium channels. Location of protonation site and dependence of proton-induced current fluctuations on concentration and species of permeant ion. Calcium channel current of vascular smooth muscle cells: extracellular protons modulate gating and single channel conductance Structural determinants of ion selectivity in brain calcium channel. Single amino acid substitutions within the ion permeation pathway alter single-channel conductance of the human L-type cardiac Ca2+ channel. Differential contribution by conserved glutamate residues to an ion-selectivity site in the L-type Ca2+ channel pore Nuclear magnetic resonance studies of lipid hydration in monomethyldioleoylphosphatidylethanolamine dispersions Interactions of protons with single open L-type calcium channels. pH dependence of proton-induced current fluctuations with Cs+, K+, and Na+ as permeant ions Two identical noninteracting sites in an ion channel revealed by proton transfer Conformational changes associated with ion permeation in L-type calcium channels Direct measurement of proton transfer rates to a group controlling the dihydropyridine-sensitive Ca2+ channel Molecular determinants of Ca2+ channel function and drug action
author name string	wds:Q71514572-3A9EC880-D8D6-463F-8806-393C321DAD29 wds:Q71514572-7B7B808B-0647-4530-8561-CA78F51CBD51 wds:Q71514572-D65BD14E-0DDF-4919-8815-AC015A3D7204 wds:Q71514572-FF1D6D53-038E-4EB2-B055-6936B4CD7424
author name string	G Mikala A Schwartz U Klöckner G Varadi
rdfs:label	Molecular studies of the asymmetric pore structure of the human cardiac voltage- dependent Ca2+ channel. Conserved residue, Glu-1086, regulates proton-dependent ion permeation (en) Molecular studies of the asymmetric pore structure of the human cardiac voltage- dependent Ca2+ channel. Conserved residue, Glu-1086, regulates proton-dependent ion permeation (nl)
skos:prefLabel	Molecular studies of the asymmetric pore structure of the human cardiac voltage- dependent Ca2+ channel. Conserved residue, Glu-1086, regulates proton-dependent ion permeation (en) Molecular studies of the asymmetric pore structure of the human cardiac voltage- dependent Ca2+ channel. Conserved residue, Glu-1086, regulates proton-dependent ion permeation (nl)
name	Molecular studies of the asymmetric pore structure of the human cardiac voltage- dependent Ca2+ channel. Conserved residue, Glu-1086, regulates proton-dependent ion permeation (en) Molecular studies of the asymmetric pore structure of the human cardiac voltage- dependent Ca2+ channel. Conserved residue, Glu-1086, regulates proton-dependent ion permeation (nl)
title	wds:Q71514572-8AB7DE4B-9690-4EAF-ACE6-DBB00FFD4CE3
title	Molecular studies of the asymmetric pore structure of the human cardiac voltage- dependent Ca2+ channel. Conserved residue, Glu-1086, regulates proton-dependent ion permeation (en)
page(s)	wds:Q71514572-E56F4DAC-9B85-4016-A16B-203C19FF06FC
page(s)	22293-22296
instance of	wds:Q71514572-3ACC0DCE-B173-4218-8468-38F60BDA67D0
instance of	scholarly article
main subject	wds:Q71514572-D67D8498-3D4A-4B02-86EA-DE48BF18A679
main subject	voltage
PubMed ID	wds:Q71514572-DA8EF9FA-49AA-46DB-AB3C-48E1C8BBE847
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8798385
PubMed ID	8798385
published in	wds:Q71514572-3BA3C171-FE7A-48C6-8E52-2C3B4400491D
published in	Journal of Biological Chemistry
issue	wds:Q71514572-D67EFBA5-6E53-48AA-85A1-2B98B0B4BC6F
volume	wds:Q71514572-B24D70D3-14F8-4FAF-BA8D-ACC18192EC5D
issue	37
volume	271
DOI	wds:Q71514572-34374FBC-DD13-40F1-9769-446AEF95ACBA
DOI	http://dx.doi.org/10.1074/JBC.271.37.22293
DOI	10.1074/JBC.271.37.22293
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q71514572
is cites work of	Overview of voltage-dependent calcium channels Acidic amino acids impart enhanced Ca2+ permeability and flux in two members of the ATP-gated P2X receptor family Architecture of Ca(2+) channel pore-lining segments revealed by covalent modification of substituted cysteines. The L-type calcium channel in the heart: the beat goes on Ion interactions in the high-affinity binding locus of a voltage-gated Ca(2+) channel Amino acid substitutions in the pore of the Ca(V)1.2 calcium channel reduce barium currents without affecting calcium currents Aspartate substitutions establish the concerted action of P-region glutamates in repeats I and III in forming the protonation site of L-type Ca2+ channels Extracellular Ca2+ modulates the effects of protons on gating and conduction properties of the T-type Ca2+ channel alpha1G (CaV3.1) pH modification of human T-type calcium channel gating Two sets of amino acids of the domain I of Cav2.3 Ca(2+) channels contribute to their high sensitivity to extracellular protons Extracellular pH Modulates the Voltage-dependent Ca2+ Current and Low Threshold K+ Current in Hair Cells The EEEE locus is the sole high-affinity Ca(2+) binding structure in the pore of a voltage-gated Ca(2+) channel: block by ca(2+) entering from the intracellular pore entrance. Enzymatic characterization of the major phospholipase A2 component of sea anemone (Aiptasia pallida) nematocyst venom
is cites work of	wds:Q34351098-9DA296F2-FE4F-491E-97CD-B193DC3ED507 wds:Q36295984-E6ED92F1-B7F8-4EEB-A1EE-9A1058634761 wds:Q48886090-1EA5D2BA-A838-48F1-B241-061B9C24DBFB wds:Q73574626-46CA7090-7ABD-43E9-BD16-6FFA27FDE8E6

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